This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tan, P S Articles by Konings, W N Search for Related Content PubMed PubMed Citation Articles by Tan, P S Articles by Konings, W N Agricola Articles by Tan, P S Articles by Konings, W N

 Previous Article  |  Next Article 

Appl Environ Microbiol. 1993 May; 59(5): 1430-1436

Degradation and debittering of a tryptic digest from beta-casein by aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2.

Department of Microbiology, University of Groningen, Haren, The Netherlands.

ABSTRACT

The mode of action of purified aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2 on a complex peptide mixture of a tryptic digest from bovine beta-casein was analyzed. The oligopeptides produced in the tryptic digest before and after aminopeptidase N treatment were identified by analysis of the N- and C-terminal amino acid sequences and amino acid compositions of the isolated peptides and by on-line liquid chromatography-mass spectrometry. Incubation of purified peptides with aminopeptidase N resulted in complete hydrolysis of many peptides, while others were only partially hydrolyzed or not hydrolyzed. The tryptic digest of beta-casein exhibits a strong bitter taste, which corresponds to the strong hydrophobicity of several peptides in the tryptic digest of beta-casein. The degradation of the "bitter" tryptic digest by aminopeptidase N resulted in a decrease of hydrophobic peptides and a drastic decrease of bitterness of the reaction mixture.

This article has been cited by other articles:

• Maehashi, K., Matano, M., Nonaka, M., Udaka, S., Yamamoto, Y. (2008). Riboflavin-Binding Protein Is a Novel Bitter Inhibitor. Chem Senses 33: 57-63 [Abstract] [Full Text]  
• Christensen, J. E., Broadbent, J. R., Steele, J. L. (2003). Hydrolysis of Casein-Derived Peptides {alpha}S1-Casein(f1-9) and {beta}-Casein(f193-209) by Lactobacillus helveticus Peptidase Deletion Mutants Indicates the Presence of a Previously Undetected Endopeptidase. Appl. Environ. Microbiol. 69: 1283-1286 [Abstract] [Full Text]  
• Tuler, T. R., Callanan, M. J., Klaenhammer, T. R. (2002). Overexpression of Peptidases in Lactococcus and Evaluation of Their Release from Leaky Cells. J DAIRY SCI 85: 2438-2450 [Abstract] [Full Text]  
• Chavagnat, F., Casey, M. G., Meyer, J. (1999). Purification, Characterization, Gene Cloning, Sequencing, and Overexpression of Aminopeptidase N from Streptococcus thermophilus A. Appl. Environ. Microbiol. 65: 3001-3007 [Abstract] [Full Text]  
• Meijer, W., van de Bunt, B., Twigt, M., de Jonge, B., Smit, G., Hugenholtz, J. (1998). Lysis of Lactococcus lactis subsp. cremoris SK110 and Its Nisin-Immune Transconjugant in Relation to Flavor Development in Cheese. Appl. Environ. Microbiol. 64: 1950-1953 [Abstract] [Full Text]